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Published on July 24, 2003; 10.1104/pp.103.020024

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Received January 7, 2003
Returned for revision January 28, 2003
Accepted April 28, 2003

Purification and Characterization of Four {beta}-Expansins (Zea m 1 Isoforms) from Maize Pollen

Lian-Chao Li , Patricia A. Bedinger , Carol Volk , A. Daniel Jones , and Daniel J. Cosgrove *

Department of Biology, 208 Mueller Laboratory (L.-C.L., D.J.C.) and Department of Chemistry, 152 Davey Laboratory (A.D.J.), The Pennsylvania State University, University Park, Pennsylvania 16802; and Department of Biology, Colorado State University, Fort Collins, Colorado 80523 (P.A.B., C.V.).

* Corresponding author; email: dcosgrove{at}psu.edu.

Four proteins with wall extension activity on grass cell walls were purified from maize (Zea mays) pollen by conventional column chromatography and high-performance liquid chromatography. Each is a basic glycoprotein (isoelectric point = 9.1-9.5) of approximately 28 kD and was identified by immunoblot analysis as an isoform of Zea m 1, the major group 1 allergen of maize pollen and member of the {beta}-expansin family. Four distinctive cDNAs for Zea m 1 were identified by cDNA library screening and by GenBank analysis. One pair (GenBank accession nos. AY104999 and AY104125) was much closer in sequence to well-characterized allergens such as Lol p 1 and Phl p 1 from ryegrass (Lolium perenne) and Phleum pretense, whereas a second pair was much more divergent. The N-terminal sequence and mass spectrometry fingerprint of the most abundant isoform (Zea m 1d) matched that predicted for AY197353, whereas N-terminal sequences of the other isoforms matched or nearly matched AY104999 and AY104125. Highly purified Zea m 1d induced extension of a variety of grass walls but not dicot walls. Wall extension activity of Zea m 1d was biphasic with respect to protein concentration, had a broad pH optimum between 5 and 6, required more than 50 µg mL-1 for high activity, and led to cell wall breakage after only approximately 10% extension. These characteristics differ from those of {alpha}-expansins. Some of the distinctive properties of Zea m 1 may not be typical of {beta}-expansins as a class but may relate to the specialized function of this {beta}-expansin in pollen function.




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